Surimi products have unsatisfactory gel properties. Hence, this study evaluates the effect of collagen-adding on surimi gel properties and provides the first observation results regarding collagen type influence. With higher water solubility and more charged amino acids than type II, collagen type I intertwines with surimi myofibrillar proteins better to induce higher exposure of protein functional domains, more sufficient conformational changes of myosin and greater formation of chemical forces among proteins. These enhancements accelerate the gelation rate, leading to a well-stabilized surimi gel. The collagen I-containing surimi gels show more compact structures with uniformly distributed smaller pores than those containing collagen II, thereby providing the final products with higher water holding capacity and better textural profiles. As such, the surimi gel fortification performance of collagen I and the well-elucidated collagen-myofibrillar protein interaction mechanism will guide the further exploitation of collagen as an effective additive in the food industry.

鱼糜产品的凝胶性能不能令人满意。因此，本研究评估了添加胶原蛋白对鱼糜凝胶特性的影响，并提供了有关胶原蛋白类型影响的第一个观察结果。与 II 型相比，I 型胶原具有更高的水溶性和更多带电荷的氨基酸，与鱼糜肌原纤维蛋白更好地缠绕在一起，从而诱导更多的蛋白质功能域暴露，更充分的肌球蛋白构象变化和蛋白质之间更多的化学力形成。这些改进加速了胶凝速率，从而产生了稳定良好的鱼糜凝胶。含有胶原蛋白 I 的鱼糜凝胶比含有胶原蛋白 II 的凝胶具有更紧凑的结构和均匀分布的更小的孔隙，从而为最终产品提供更高的持水能力和更好的质地。像这样，